US6323319B1 - Method of making hydrolyzed collagen type II - Google Patents
Method of making hydrolyzed collagen type II Download PDFInfo
- Publication number
- US6323319B1 US6323319B1 US09/453,302 US45330299A US6323319B1 US 6323319 B1 US6323319 B1 US 6323319B1 US 45330299 A US45330299 A US 45330299A US 6323319 B1 US6323319 B1 US 6323319B1
- Authority
- US
- United States
- Prior art keywords
- collagen type
- cartilage
- hydrolysate
- hydrolyzed collagen
- powder
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Definitions
- the present invention relates to a method of preparing hydrolyzed collagen type II and its use as a therapeutic agent and nutritional supplement.
- Collagen is a complex structural protein which provides strength and flexibility to skin, hair and nails. Collagen is an essential and major component of muscles, tendons, cartilage, ligaments, joints and blood vessels. There are three main types of collagen: I, II and III. Types I and III are primarily found in skin, tendon and bone. In contrast, type II is found predominantly in particular cartilage. Collagen is an unusual protein, in that the proportion of glycine residues is nearly one-third which is unusually high. Proline is also present to a much greater extent in collagen than in most other proteins. Moreover, collagen contains two amino acids, 4-hydroxyproline and 5-hydroxylysine, that are found in very few other proteins. The amnino acid sequence of collagen is remarkably regular, nearly every third amino acid being glycine.
- Collagen a mixture of Types I, II
- Collagen Beauty SupplementTM Smarter Nails & Hair, Inc., Newport Beach, Calif.
- “Hydrolyzed, Collagen Beauty Supplement TabletTM” Smarter Nails & Hair, Inc., Newport Beach, Calif.
- U.S. Pat. No. 4,804,745 to Koepff et al. discloses agents containing collagen peptides produced by enzymatic hydrolysis for the treatment of degenerative joint diseases. These peptides can be obtained from animal skin, animal bones and other sufficiently purified connective tissue and have average molecular weights of between 30 and 45 kilodaltons.
- U.S. Pat. No. 5,364,845 to Henderson discloses a therapeutic composition and method for the protection, treatment and repair of connective tissue in mammals.
- This composition comprises glucosamine, chondroitin sulfate and manganese ascorbate.
- U.S. Pat. No. 5,587,363 to Henderson discloses a therapeutic composition and method for the protection, treatment and repair of connective tissue in mammals which includes aminosugars and glycosaminoglycans.
- compositions capable of promoting repair of damaged connective tissue There is a constant need for compositions capable of promoting repair of damaged connective tissue.
- the present invention addresses this need.
- One embodiment of the present invention is hydrolyzed collagen type II, the hydrolyzed collagen having an average molecular weight of between about 1,500 and 2,500 daltons.
- the hydrolyzed collagen type II has an average molecular weight of about 1,800 daltons.
- the collagen is obtained from chicken sternal cartilage.
- the present invention also provides a method of inducing cartilage formation in an individual with a connective tissue disorder, comprising orally administering to the individual an effective daily cartilage-inducing amount of hydrolyzed collagen type II.
- the connective tissue disorder includes degenerative joint diseases, joint defects, osteoarthritis, polychondritis, vascular disease and cartilage injuries.
- the effective daily amount is between about 500 and 5,000 mg. More preferably, the effective daily amount is between about 1,000 and 4,000 mg. Most preferably, the effective daily amount is between about 2,000 and 3,000 mg.
- Another embodiment of the invention is a method of providing collagen type II as a nutritional supplement, comprising orally administering to an individual a daily dosage of hydrolyzed collagen having an average mole weight of between about 1,500 and 2,500 daltons.
- Still another embodiment of the invention is a method of preparing hydrolyzed collagen type II powder, comprising the following steps: cutting fresh chicken sternal cartilage to within not less than about 2 mm of the bone; suspending tho cartilage in an aqueous solution; treating said cartilage with a proteolytic enzyme to form a hydrolysate; sterilizing the hydrolysate; filtering the hydrolysate; concentrating the hydrolysate; and drying the hydrolysate to form a collagen type II powder.
- the method may further comprise the step of freezing the cartilage after the cutting step.
- the aqueous solution is water.
- the enzyme is papain, ficin or bromelain.
- the sterilizing step comprises heating the hydrolysate at 95° C. for about 30 minutes.
- the drying step comprises spray drying.
- the pH of the suspending and treating steps is between about 4 and 8.
- FIG. 1 is a schematic diagram of the process for preparing the hydrolyzed collagen type II powder of the invention.
- the present invention provides a hydrolyzed, denatured collagen type II composition, method for preparing the composition and use of the composition in the prevention, treatment and repair of cartilage defects.
- the method involves cutting fresh sternal cartilage from chicken carcasses and removing all meat therefrom.
- the sternal cartilage is cut, leaving a space of about two millimeters from the bone so as to not remove any bone fragments. This is critical to the purity of the fmal product because it avoids contamination of collagen type II with types I and III found in bone.
- the fresh sternal cartilage is then promptly frozen and the remained of the chicken carcass is discarded. It is exclusively the sternal cartilage, cut so no bone is included, that is used for preparing the collagen type II powder.
- the chicken sternal cartilage is processed according to good manufacturing procedures (GMP).
- Other contemplated sources of collagen type II are mammalian curfilage (i.e. bovine and porcine) and shark fins.
- FIG. 1 The production of hydrolyzed collagen type II in powdered form is shown in FIG. 1 .
- Whole cartilage is suspended in an aqueous solution, preferably water for about one hour at about 35° C. at a pH of between about 4 and 8.
- the pH is between about 6 and 7.
- the pH is about 6.5.
- the water is removed, and the cartilage is incubated with one or more proteases obtainable from a natural source (i.e. papain, ficin, bromelain) for between about 2 and 10 hours, preferably about 6 hours, at about 35° C.-55° C. at a pH of between about 4 and 8 to form a hydrolysate.
- a natural source i.e. papain, ficin, bromelain
- the pH will depend on the pH optimum of the particular enzyme(s) used for the hydrolysis and are well known to one of ordinary skill in the art.
- the hydrolysate is then sterilized for about 30 minutes at a temperature between about 95° C. and 105° C.
- the sterilized hydrolysate is filtered through diatomaceous earth, concentrated, preferably under vacuum, dried to form a powder and packed. Other filtration methods are contemplated, including vacuum filtration.
- the hydrolyzed collagen type II is spray dried using a size 56 pressure nozzle into a heat tunnel. The final particle size and mesh are adjusted to 0.46 g/cc, yielding a fine powder.
- the powder is packed in a 40 kg drum with a plastic bag liner.
- the powder is water soluble.
- the average molecular weight of the final product is between 1,500 and 2,500 daltons, preferably 1,800 daltons.
- the moisture content is between 5% and 7%.
- the final product is high in mucopolysaccharides, particularly chondroitin sulfate and glucosamine sulfate.
- the product has 375 calories per 100 grams, contains 67% protein (12.1% total nitrogen), 18% carbohydrate and 0.1% fat.
- the amino acid composition of the hydrolysate differs substantially from typical collagens and is shown in Table 1. Hydroxyproline is low, hydroxylysine is absent and tryptophan is low. The molecular weight and amino acid composition promote optimal assimilation of the peptides.
- hydrolyzed collage type II When taken orally by an individual with a connective tissue disorder, hydrolyzed collage type II helps build cartilage and significantly improves the disorder.
- “Oral” administration includes oral, enteral or intragastric administration.
- the hydrolyzed collagen type II of the invention can be used to treat, for example, degenerative joint diseases (i.e. rheumatoid arthritis), joint defects, osteoarthritis, polychondritis, vascular disease, cartilage injuries, silicone poisoning due to ruptured breast implants, autoimmune diseases involving connective tissue autoantibodies (i.e. rheumatoid arthritis), progressive myopia, Menier's disease and any other connective tissue disorder which would benefit from increased synthesis of cartilage.
- the hydrolyzed collagen type II also significantly reduces sun-induced skin wrinkles.
- the hydrolyzed collagen type II of the invention may be provided as a dispersible powder or granule, tablet, aqueous or oil suspension, emulsion, hard or soft capsule, syrup or elixir.
- Compositions intended for oral use may be prepared according to any method known in the art for the manufacture of pharmaceutical compositions and such compositions may contain one or more of the following agents: sweeteners, flavoring agents, coloring agents and preservatives. The sweetening and flavoring agents will increase the palatability of the preparation. Tablets containing the hydrolyzed collagen type II in admixture with non-toxic pharmaceutically acceptable excipients stable for tablet manufacture are acceptable.
- excipients include inert diluents such as calcium carbonate, sodium carbonate, lactose, calcium phosphate or sodium phosphate; granulating and disintegrating agents, such as corn starch or alginic acid; binding agents such as starch, gelatin or acacia; and lubricating agents such as magnesium stearate, stearic acid or talc. Tablets may be uncoated or may be coated by known techniques to delay disintegration and absorption in the gastrointestinal tract and thereby provide a sustained action over a longer period of time. For example, a time delay material such as glyceryl monostearate or glyceryl distearate alone or with a wax may be employed. The use of enteric coatings is also contemplated.
- Formulations for oral use may also be presented as hard gelatin capsules wherein the active ingredient is mixed with an inert solid diluent, for example calcium carbonate, calcium phosphate or kaolin, or as soft gelatin capsules wherein the active ingredient is mixed with water or an oil medium, such as peanut oil, liquid paraffin or olive oil.
- an inert solid diluent for example calcium carbonate, calcium phosphate or kaolin
- an oil medium such as peanut oil, liquid paraffin or olive oil.
- Aqueous suspensions may contain the hydrolyzed collage type II of the invention in admixture with excipients suitable for the manufacture of aqueous suspensions.
- excipients include suspending agents, dispersing or wetting agents, one or more preservatives, one or more coloring agents, one or more flavoring agents and one or more sweetening agents such as sucrose or saccharin.
- Oil suspensions may be formulated by suspending the active ingredient in a vegetable oil, such as arachis oil, olive oil, sesame oil or coconut oil, or in a mineraloil such as liquid paraffin.
- the oil suspension may contain a thickening agent, such as beeswax, hard paraffin or cetyl alcohol.
- Sweetening agents such as those set forth above, and flavoring agents may be added to provide a palatable oral preparation. These compositions may be preserved by an added antioxidant such as ascorbic acid.
- Dispersible powers and granules of the invention sable for preparation of am aqueous suspension by the addition of water provide the active ingredient in admixture with a dispersing or wetting agent, a suspending agent, and one or more preservatives. Additional excipients, for example sweetening, flavoring and coloring agents, may also be present.
- Syrups and elixirs may be formulated with sweetening agents, such as glycerol, sorbitol or sucrose. Such formulations may also contain a demulcent, a preservative, a flavoring agent and/or a coloring agent.
- sweetening agents such as glycerol, sorbitol or sucrose.
- Such formulations may also contain a demulcent, a preservative, a flavoring agent and/or a coloring agent.
- the hydrolyzed collagen type II powder may be mixed with other ingestible forms and consumed in solid, semi-solid solution, suspension or emulsion form. It may also be mixed in conjunction or alternatively with pharmaceutically acceptable carriers, flavor enhancers, water, suspending agents and emulsifying agents.
- the hydrolyzed collagen type II powder is mixed with a citrus juice such as orange, grapefruit or tangerine due to the promotion of connective tissue formation by ascorbic acid.
- the hydrolyzed collagen may also be provided in tablet form in admixture with ascorbic acid.
- the hydrolyzed collagen is orally administered in a daily dosage of between about 500 mg and 5,000 mg. More preferably, it is administered in a daily dosage of between about 2,000 mg and 4,000 mg. Most preferably, it is administered in a daily dosage of between about 2,000 and 3,000 mg per day.
- the hydrolyzed collagen type II powder may be formulated into tablets which range from 300 mg to 1,000 mg per tablet.
- the hydrolyzed collage type II powder is formulated into 500 mg tablets and 4-6 tablets are taken daily.
- the tablets are taken on an empty stomach with a beverage containing vitamin C.
- the hydrolyzed collagen type II powder is mixed with water or a citrus juice prior to ingestion.
- the preparations described above can be taken indefinitely by individuals affected by connective tissue disorders or by healthy individuals as a preventative agent. If desired, an individual with such a disorder can take the preparation until no further improvement is noted in the disorder.
Abstract
Description
TABLE 1 |
Amino acid composition of hydrolyzed collagen type II |
Amino acid | g/100 g product | ||
arginine | 4.42 | ||
histidine | 2.05 | ||
isoleucine | 1.90 | ||
leucine | 4.20 | ||
lysine | 3.54 | ||
methionine | 1.38 | ||
phenylalanine | 2.14 | ||
threonine | 2.60 | ||
tryptophan | 0.37 | ||
alanine | 4.51 | ||
asparagine/aspartic acid | 5.29 | ||
cystine | 0.46 | ||
glutamine/glutamic acid | 8.75 | ||
glycine | 8.93 | ||
hydroxyproline | 3.90 | ||
proline | 5.25 | ||
serine | 2.45 | ||
tyrosine | 1.16 | ||
valine | 2.43 | ||
Claims (8)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US09/453,302 US6323319B1 (en) | 1997-08-08 | 1999-12-02 | Method of making hydrolyzed collagen type II |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US08/907,735 US6025327A (en) | 1997-08-08 | 1997-08-08 | Hydrolyzed collagen type II and use thereof |
US09/453,302 US6323319B1 (en) | 1997-08-08 | 1999-12-02 | Method of making hydrolyzed collagen type II |
Related Parent Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US08/907,735 Continuation US6025327A (en) | 1997-08-08 | 1997-08-08 | Hydrolyzed collagen type II and use thereof |
Publications (1)
Publication Number | Publication Date |
---|---|
US6323319B1 true US6323319B1 (en) | 2001-11-27 |
Family
ID=25424560
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US08/907,735 Expired - Lifetime US6025327A (en) | 1997-08-08 | 1997-08-08 | Hydrolyzed collagen type II and use thereof |
US09/453,302 Expired - Lifetime US6323319B1 (en) | 1997-08-08 | 1999-12-02 | Method of making hydrolyzed collagen type II |
Family Applications Before (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US08/907,735 Expired - Lifetime US6025327A (en) | 1997-08-08 | 1997-08-08 | Hydrolyzed collagen type II and use thereof |
Country Status (1)
Country | Link |
---|---|
US (2) | US6025327A (en) |
Cited By (18)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US20030091652A1 (en) * | 2001-11-13 | 2003-05-15 | Suhail Ishaq | Hyaluronic acid and chondroitin sulfate based hydrolyzed collagen type II and method of making same |
US20040029774A1 (en) * | 2002-08-06 | 2004-02-12 | Aly Gamay | Composition and methods for the treatment of musculoskeletal disorders and collagen and elastin deficiencies |
WO2004052910A1 (en) * | 2002-11-14 | 2004-06-24 | Affiliated Hospital Of Academy Of Military Medical Sciences, Pla | A full-length polynucleotide coding chicken type ii collagen and the use of it |
FR2900155A1 (en) * | 2006-04-21 | 2007-10-26 | Diana Naturals Sa | Avian cartilage hydrolyzate, useful e.g. to treat/prevent joint pain, comprises hydrolyzed type II collagen, chondroitin sulfate, hyaluronic acid and amino acids e.g. phenylalanine, lysine, tryptophan, hydroxyproline and hydroxylysine |
WO2007122179A1 (en) * | 2006-04-21 | 2007-11-01 | Diana Naturals | Hydrolysate of avian cartilage, process of preparation and uses thereof |
WO2014118271A1 (en) | 2013-01-31 | 2014-08-07 | Sochim International S.P.A. | Compositions for oral administration having a beneficial effect on cartilage disease, osteoarthritis and joint disease with an inflammatory component |
US20150283303A1 (en) * | 2012-10-29 | 2015-10-08 | Scripps Health | Methods of transplanting chondrocytes |
WO2015171300A1 (en) * | 2014-05-05 | 2015-11-12 | Napier Consulting Llc | Compositions and methods for hair growth |
US9914911B2 (en) | 2012-10-29 | 2018-03-13 | Scripps Health | Methods of reprogramming chondrocytes |
US20190022590A1 (en) * | 2017-07-21 | 2019-01-24 | Titan Biological & Agricultural Technology Co., Ltd. | Device for separation and purification of collagen type 2 in chicken bones |
US10226513B2 (en) | 2015-01-09 | 2019-03-12 | Mark Terrell Smith | Method and composition to prevent or improve symptoms of musculoskeletal distress degeneration |
US10253090B2 (en) | 2016-03-22 | 2019-04-09 | Avicenna Nutraceutical, Llc | Hydrolyzed collagen compositions and methods of making thereof |
US10555967B2 (en) * | 2013-07-08 | 2020-02-11 | International Dehydrated Foods, Inc. | Compositions prepared from poultry and methods of their use |
US10724005B2 (en) | 2012-09-28 | 2020-07-28 | Scripps Health | Methods of differentiating stem cells into chondrocytes |
US11478504B2 (en) | 2013-07-08 | 2022-10-25 | International Dehydrated Foods, Inc. | Compositions and methods for preventing/treating metabolic syndrome |
US20220401525A1 (en) * | 2021-06-16 | 2022-12-22 | Biocell Technology, Llc | Use of collagen compositions for increasing telomere length |
US11702447B2 (en) | 2017-05-11 | 2023-07-18 | Avicenna Nutraceutical, Inc. | Methods for producing collagen |
EP4084868A4 (en) * | 2019-12-27 | 2024-01-31 | Suntory Holdings Ltd | Food or beverage composition containing peptide and/or salt thereof, production method thereof, use of hydrolyzed collagen type ii, composition for inhibiting bone resorption, and use of chicken extract |
Families Citing this family (30)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6838440B2 (en) * | 2001-01-24 | 2005-01-04 | Collagen Nutraceuticals, Inc. | Kolla2-desiccated avian sternal cartilage powder |
JP2005519914A (en) | 2002-01-23 | 2005-07-07 | インスティチュート オブ ニュートラシューティカル リサーチ ピーティーワイ リミテッド | Nutraceuticals for the treatment, protection and recovery of connective tissue |
AU2003903037A0 (en) * | 2003-06-17 | 2003-07-03 | Institute Of Nutraceutical Research | Connective tissue derived polypeptides |
EP3508201A3 (en) * | 2004-08-09 | 2019-10-16 | Enrique Melendez Hevia | Glycine as a diet supplement for use in the treatment skin problems that result from underlying collagen disorders and and cosmetic uses thereof |
WO2007044945A2 (en) * | 2005-10-13 | 2007-04-19 | Gu, Jennifer, L. | Mineral collagen chelates and methods of making and using same |
CA2669524C (en) * | 2006-11-15 | 2015-02-17 | Meiji Seika Kaisha, Ltd. | Collagen peptide composition and food or beverage containing the same |
US9402857B2 (en) | 2009-07-23 | 2016-08-02 | U.S. Nutraceuticals, LLC | Composition and method to alleviate joint pain using low molecular weight hyaluronic acid and astaxanthin |
US9913810B2 (en) | 2009-07-23 | 2018-03-13 | U.S. Nutraceuticals, LLC | Composition and method to alleviate joint pain using phospholipids and astaxanthin |
US9399047B2 (en) | 2009-07-23 | 2016-07-26 | U.S. Nutraceuticals, LLC | Composition and method to alleviate joint pain using phospholipids and roe extract |
US20110217370A1 (en) * | 2010-03-04 | 2011-09-08 | Joar Opheim | Substances for promoting healthy joint function comprising glucosamine sulfate, omega-3 polyunsaturated fatty acids or derivatives thereof, and undenatured type ii collagen |
US20110218151A1 (en) * | 2010-03-04 | 2011-09-08 | Joar Opheim | Substances for promoting healthy joint function comprising omega-3 polyunsaturated fatty acids or drivatives thereof, undenatured type ii collagen and, optionally, glucosamine sulfate |
DE102010060564A1 (en) | 2010-11-15 | 2012-05-16 | Gelita Ag | Use of collagen hydrolyzate to improve the health of human skin, hair and / or nails |
US8344106B1 (en) * | 2011-08-03 | 2013-01-01 | Robert den Hoed | Collagen mixture and method of making the same |
US20130217631A1 (en) * | 2011-08-03 | 2013-08-22 | Molecular Biology International, Inc. | Collagen mixture and method of making the same |
US20130079496A1 (en) * | 2011-08-03 | 2013-03-28 | Dana Summers | Collagen mixture and method of making the same |
KR20160144388A (en) | 2014-03-18 | 2016-12-16 | 유.에스. 뉴트라수티칼스, 엘.엘.씨. | Composition and method to alleviate joint pain using low molecular weight hyaluronic acid and astaxanthin |
DE212015000073U1 (en) | 2014-03-18 | 2016-12-06 | U.S. Nutraceuticals Llc Dba Valensa International | Composition for relieving joint pain with phospholipids and astaxanthin |
WO2015142702A1 (en) | 2014-03-18 | 2015-09-24 | U.S. Nutraceuticals, Llc D/B/A Valensa International | Composition and method to alleviate joint pain using phospholipids and roe extract |
DE212015000031U1 (en) | 2014-05-13 | 2017-02-20 | U.S. Nutraceuticals, Llc D/B/A Valensa International | Composition that uses seed oil extracts and phospholipids to improve the absorption of carotenoids |
DE102014108502A1 (en) * | 2014-06-17 | 2015-12-17 | Gelita Ag | Composition in the form of compacted particles and their use |
DK3053458T3 (en) | 2015-01-28 | 2020-02-03 | Paninkret Chemisch Pharmazeutisches Werk Gmbh | Spray-dried composition comprising an acerola fruit extract, hydrolyzed collagen type II and chondroitin sulfate |
GB201511255D0 (en) * | 2015-06-26 | 2015-08-12 | Colltec Ltd | Formulation |
AU2017361805B2 (en) * | 2016-11-16 | 2022-04-21 | Fresenius Kabi Deutschland Gmbh | Nutritional composition for use in therapy of cancer patients |
WO2018166807A1 (en) * | 2017-03-15 | 2018-09-20 | Rousselot B.V. | Compositions of hydrolyzed collagen peptides and commensal microorganisms and methods thereof |
AR114928A1 (en) * | 2017-05-17 | 2020-11-11 | Americo Puppo | FOOD ADDITIVE TO IMPROVE SENSORY CHARACTERISTICS AND PROVIDE NUTRITIONAL VALUE IN CEREALS OR MIXTURE OF CEREALS WITH IRREGULAR SURFACE, PROCESS FOR OBTAINING THE ADDITIVE AND PROCESS FOR OBTAINING CEREALS OR CEREAL ADDITION MIXTURE |
US20180339085A1 (en) * | 2017-05-24 | 2018-11-29 | In2Bones Usa, Llc | System and methods for soft-tissue augmentation |
WO2019083732A1 (en) | 2017-10-23 | 2019-05-02 | U.S. Nutraceuticals, Llc D/B/A Valensa International | Composition to treat in humans photo-induced ocular fatigue and associated reduction in speed of ocular focus |
WO2019226186A1 (en) | 2018-05-24 | 2019-11-28 | U.S. Nutraceuticals, Llc D/B/A Valensa International | Composition and method to alleviate joint pain using hyaluronic acid and eggshell membrane components |
DE202018105422U1 (en) | 2018-06-21 | 2018-10-19 | U.S. Nutraceuticals, Llc D/B/A Valensa International | A composition for relieving joint pain using hyaluronic acid and egg shell membrane components |
CA3164511A1 (en) | 2020-01-13 | 2021-07-22 | Chathurada GAJADEERA | Turkey collagen hydrolysates and methods of making |
Citations (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4511653A (en) | 1981-11-26 | 1985-04-16 | Foundation Merieux | Process for the industrial preparation of collagenous materials from human placental tissues, human collagenous materials obtained and their application as biomaterials |
US4804745A (en) | 1986-07-25 | 1989-02-14 | Deutsche Gelatine-Fabriken Stoess & Co. Gmbh | Agents for the treatment of arthroses |
US5206023A (en) | 1991-01-31 | 1993-04-27 | Robert F. Shaw | Method and compositions for the treatment and repair of defects or lesions in cartilage |
US5364775A (en) | 1991-11-13 | 1994-11-15 | Kyowa Hakko Kogyo Co., Ltd. | Process for producing trans-L-hydroxyproline |
US5364845A (en) | 1993-03-31 | 1994-11-15 | Nutramax Laboratories, Inc. | Glucosamine, chondroitin and manganese composition for the protection and repair of connective tissue |
US5399347A (en) | 1987-06-24 | 1995-03-21 | Autoimmune, Inc. | Method of treating rheumatoid arthritis with type II collagen |
US5645851A (en) | 1994-02-28 | 1997-07-08 | Moore; Eugene R. | Product for alleviating the symptons of arthritis in mammals |
WO1997025435A1 (en) | 1996-01-05 | 1997-07-17 | Autoimmune, Inc. | Method for preparation of type ii collagen |
-
1997
- 1997-08-08 US US08/907,735 patent/US6025327A/en not_active Expired - Lifetime
-
1999
- 1999-12-02 US US09/453,302 patent/US6323319B1/en not_active Expired - Lifetime
Patent Citations (10)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4511653A (en) | 1981-11-26 | 1985-04-16 | Foundation Merieux | Process for the industrial preparation of collagenous materials from human placental tissues, human collagenous materials obtained and their application as biomaterials |
US4804745A (en) | 1986-07-25 | 1989-02-14 | Deutsche Gelatine-Fabriken Stoess & Co. Gmbh | Agents for the treatment of arthroses |
US5399347A (en) | 1987-06-24 | 1995-03-21 | Autoimmune, Inc. | Method of treating rheumatoid arthritis with type II collagen |
US5206023A (en) | 1991-01-31 | 1993-04-27 | Robert F. Shaw | Method and compositions for the treatment and repair of defects or lesions in cartilage |
US5364775A (en) | 1991-11-13 | 1994-11-15 | Kyowa Hakko Kogyo Co., Ltd. | Process for producing trans-L-hydroxyproline |
US5364845A (en) | 1993-03-31 | 1994-11-15 | Nutramax Laboratories, Inc. | Glucosamine, chondroitin and manganese composition for the protection and repair of connective tissue |
US5587363A (en) | 1993-03-31 | 1996-12-24 | Nutramax Laboratories, Inc. | Aminosugar and glycosaminoglycan composition for the treatment and repair of connective tissue |
US5364845C1 (en) | 1993-03-31 | 2002-09-10 | Nutramax Lab Inc | Glusosamine chondroitin and manganese composition for the protection and repair of connective tissue |
US5645851A (en) | 1994-02-28 | 1997-07-08 | Moore; Eugene R. | Product for alleviating the symptons of arthritis in mammals |
WO1997025435A1 (en) | 1996-01-05 | 1997-07-17 | Autoimmune, Inc. | Method for preparation of type ii collagen |
Non-Patent Citations (13)
Title |
---|
Barinaga, Treating Arthritis With Tolerance, Science 261:1669-1670 (1993). |
Bedi et al., Purification and characterization of a collagen-degrading protease from Porphyromonas gingivalis, J. Biol. Chem. 269:599-606 (1994). |
Brucknet et al., p-HMW-Collegen, a minor collagen obtained from chick embryo cartilage without proteolytic treatment of the tissue, Eur. J. Biochem. |
Cremer et al., Collagen-Induced Arthritis in Rats: Antigen-Specific Suppression of Arthritis and Immunity By Intravenously Injected Native Type II Collagen, J. of Immun. 131(6):2995-3000 (1983). |
Darnell et al., Molecular Cell Biology, Scientific American Books, Inc. New York, NY 1986. |
Englert et al., Suppression of Type II Collagen-Induced Arthritis by the Intravenous Adminstration of Type II Collagen or Its Constituent Peptide á1(II)CB10, Cellular Immunology 87:357-365 (1984). |
Fawcett, A textbook of Histology, W.B. Ssaunders Co. Philadelphia, PA (1986). |
File Caplus on STN: No. 1984:180121. RO 80226, Nov. 30, 1982 Abstract only. |
Knauper et al., Biochemical characterization of human collagenase-3, J. Biol. Chem. 271:1544-1550 (1996). |
New Product Advertisement for "Hydrolyzed Collagen Beauty Supplement", Smarter Nails & Hair, Inc., Newport Beach, CA 92660 (1987). |
Stryer, Collagen Has An Unusual Amino Acid Composition And Sequence, Biochemistry, Third Edition, W.H. Freeman and Co., New York, p. 262 1988). |
Trentham, et al., Autoimmunity to Type II Collagen: An Experimental Model of Arthritis, J. of Exp. Medicine 146:857-868 (1977). |
Trentham, et al., Effects of Oral Administration of Type II Collagen on Rheumatoid Arthritis, Science 261:1727-1730 (1993). |
Cited By (32)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US20110034392A1 (en) * | 2001-11-13 | 2011-02-10 | Biocell Technology, Llc | Hyaluronic Acid and Chondroitin Sulfate Based Hydrolyzed Collagen Type II and Method of Making Same |
US6780841B2 (en) * | 2001-11-13 | 2004-08-24 | Biocell Technology, Llc | Hyaluronic acid and chondroitin sulfate based hydrolyzed collagen type II and method of making same |
US20040224384A1 (en) * | 2001-11-13 | 2004-11-11 | Suhail Ishaq | Hyaluronic acid and chondroitin sulfate based hydrolyzed collagen type II and method of making same |
US7091180B2 (en) * | 2001-11-13 | 2006-08-15 | Intellipi, Llc | Hyaluronic acid and chondroitin sulfate based hydrolyzed collagen type II and method of making same |
US20030091652A1 (en) * | 2001-11-13 | 2003-05-15 | Suhail Ishaq | Hyaluronic acid and chondroitin sulfate based hydrolyzed collagen type II and method of making same |
US8563045B2 (en) | 2001-11-13 | 2013-10-22 | Biocell Technology, Llc | Hyaluronic acid and chondroitin sulfate based hydrolyzed collagen type II and method of making same |
US20040029774A1 (en) * | 2002-08-06 | 2004-02-12 | Aly Gamay | Composition and methods for the treatment of musculoskeletal disorders and collagen and elastin deficiencies |
WO2004052910A1 (en) * | 2002-11-14 | 2004-06-24 | Affiliated Hospital Of Academy Of Military Medical Sciences, Pla | A full-length polynucleotide coding chicken type ii collagen and the use of it |
US7973010B2 (en) | 2002-11-14 | 2011-07-05 | Affiliated Hospital Of Academy Of Military Medical Sciences, Pla | Full length polynucleotide coding chicken type II collagen and the use of it |
FR2900155A1 (en) * | 2006-04-21 | 2007-10-26 | Diana Naturals Sa | Avian cartilage hydrolyzate, useful e.g. to treat/prevent joint pain, comprises hydrolyzed type II collagen, chondroitin sulfate, hyaluronic acid and amino acids e.g. phenylalanine, lysine, tryptophan, hydroxyproline and hydroxylysine |
US7671041B2 (en) | 2006-04-21 | 2010-03-02 | Diana Naturals | Hydrolysate of avian cartilage, process of preparation and uses thereof |
US20070293427A1 (en) * | 2006-04-21 | 2007-12-20 | Eric Vouland | Hydrolysate of avian cartilage, process of preparation and uses thereof |
WO2007122179A1 (en) * | 2006-04-21 | 2007-11-01 | Diana Naturals | Hydrolysate of avian cartilage, process of preparation and uses thereof |
US10724005B2 (en) | 2012-09-28 | 2020-07-28 | Scripps Health | Methods of differentiating stem cells into chondrocytes |
US11859210B2 (en) | 2012-09-28 | 2024-01-02 | Scripps Health | Methods of differentiating stem cells into chondrocytes |
US10385318B2 (en) | 2012-10-29 | 2019-08-20 | Scripps Health | Method of making a population of chondrocytes from reprogrammed chondrocytes |
US9974885B2 (en) * | 2012-10-29 | 2018-05-22 | Scripps Health | Methods of transplanting chondrocytes |
US20150283303A1 (en) * | 2012-10-29 | 2015-10-08 | Scripps Health | Methods of transplanting chondrocytes |
US10179193B2 (en) | 2012-10-29 | 2019-01-15 | Scripps Health | Methods of transplanting chondrocytes |
US9914911B2 (en) | 2012-10-29 | 2018-03-13 | Scripps Health | Methods of reprogramming chondrocytes |
WO2014118271A1 (en) | 2013-01-31 | 2014-08-07 | Sochim International S.P.A. | Compositions for oral administration having a beneficial effect on cartilage disease, osteoarthritis and joint disease with an inflammatory component |
US10555967B2 (en) * | 2013-07-08 | 2020-02-11 | International Dehydrated Foods, Inc. | Compositions prepared from poultry and methods of their use |
US11419890B2 (en) * | 2013-07-08 | 2022-08-23 | International Dehydrated Foods, Inc. | Compositions prepared from poultry and methods of their use |
US11478504B2 (en) | 2013-07-08 | 2022-10-25 | International Dehydrated Foods, Inc. | Compositions and methods for preventing/treating metabolic syndrome |
WO2015171300A1 (en) * | 2014-05-05 | 2015-11-12 | Napier Consulting Llc | Compositions and methods for hair growth |
US10226513B2 (en) | 2015-01-09 | 2019-03-12 | Mark Terrell Smith | Method and composition to prevent or improve symptoms of musculoskeletal distress degeneration |
US10253090B2 (en) | 2016-03-22 | 2019-04-09 | Avicenna Nutraceutical, Llc | Hydrolyzed collagen compositions and methods of making thereof |
US11028147B2 (en) | 2016-03-22 | 2021-06-08 | Avicenna Nutraceutical, Llc | Hydrolyzed collagen compositions and methods of making thereof |
US11702447B2 (en) | 2017-05-11 | 2023-07-18 | Avicenna Nutraceutical, Inc. | Methods for producing collagen |
US20190022590A1 (en) * | 2017-07-21 | 2019-01-24 | Titan Biological & Agricultural Technology Co., Ltd. | Device for separation and purification of collagen type 2 in chicken bones |
EP4084868A4 (en) * | 2019-12-27 | 2024-01-31 | Suntory Holdings Ltd | Food or beverage composition containing peptide and/or salt thereof, production method thereof, use of hydrolyzed collagen type ii, composition for inhibiting bone resorption, and use of chicken extract |
US20220401525A1 (en) * | 2021-06-16 | 2022-12-22 | Biocell Technology, Llc | Use of collagen compositions for increasing telomere length |
Also Published As
Publication number | Publication date |
---|---|
US6025327A (en) | 2000-02-15 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
US6323319B1 (en) | Method of making hydrolyzed collagen type II | |
CA2435392C (en) | Desiccated avian sternal cartilage powder | |
US7091180B2 (en) | Hyaluronic acid and chondroitin sulfate based hydrolyzed collagen type II and method of making same | |
AU718253B2 (en) | Basic protein composition, basic peptide composition and application thereof | |
JPH0696539B2 (en) | Joint remedies | |
US20190292242A1 (en) | Hydrolyzed Jellyfish Collagen Types I, II, and V and Use Thereof | |
JP2004238365A (en) | Skin beautifying agent, and beauty and health food | |
JP2805194B2 (en) | Peptide for increasing blood triglyceride concentration and blood triglyceride concentration increase inhibitor containing the peptide as an active ingredient | |
JP3068656B2 (en) | Novel peptide and angiotensin converting enzyme inhibitory peptide and oral feeding composition containing them | |
WO2001084948A1 (en) | Compositions containing peptide and electrolyte excretion promoter and foods containing the same | |
EP3053458B1 (en) | Spray-Dried Composition Comprising an Acerola Fruit Extract, Hydrolyzed Collagen Type II and Chondroitin Sulfate | |
CA2212649C (en) | Hydrolyzed collagen type ii and use thereof | |
JP2003246741A (en) | Oral skin improver, food composition for skin improvement and skin improvement process | |
MXPA05004994A (en) | Composition for the treatment of gastrointestinal disorders. | |
JP2003245055A (en) | Skin-improving food composition and skin-improving method | |
JPH06165655A (en) | Composition for reducing cholesterol | |
JP7357189B1 (en) | Collagen-containing composition derived from fish cartilage | |
JP2001026753A (en) | Composition for prophylaxis or treatment of hypertension | |
RU2366263C2 (en) | Broth with preventive properties, containing protein hydrolisate and protein hydrolisate production method | |
JP4115561B2 (en) | Hair growth promoter | |
Elavarasan | Marine functional proteins & their application | |
JP2732056B2 (en) | Antihypertensive and vasodilator | |
JP2020110066A (en) | Blood pressure elevation depressant including chondroitin sulfate-containing pig cartilage extract as active principle and food composition containing the same | |
Дзюба et al. | COLLAGEN HYDROLYZATE AS COMPONENT OF FOODSTUFFS OF HEALTH NUTRITION | |
JPH0662423B2 (en) | Gastric mucosa protective agent containing chondroitin sulfate |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
AS | Assignment |
Owner name: FIVE CONTINENT ENTERPRISE, INC., CALIFORNIA Free format text: ASSIGNMENT OF ASSIGNORS INTEREST;ASSIGNOR:BIOCELL TECHNOLOGY, LLC;REEL/FRAME:010832/0930 Effective date: 20000515 |
|
STCF | Information on status: patent grant |
Free format text: PATENTED CASE |
|
AS | Assignment |
Owner name: BIOCELL TECHNOLOGY, LLC, CALIFORNIA Free format text: ASSIGNMENT OF ASSIGNORS INTEREST;ASSIGNOR:FIVE CONTINENT ENTERPRISE, INC.;REEL/FRAME:012573/0619 Effective date: 20011003 |
|
AS | Assignment |
Owner name: INTELLIPI, LLC, CALIFORNIA Free format text: ASSIGNMENT OF ASSIGNORS INTEREST;ASSIGNOR:BIOCELL TECHNOLOGY, LLC;REEL/FRAME:015503/0449 Effective date: 20041221 |
|
FPAY | Fee payment |
Year of fee payment: 4 |
|
FPAY | Fee payment |
Year of fee payment: 8 |
|
AS | Assignment |
Owner name: BIOCELL TECHNOLOGY, LLC, CALIFORNIA Free format text: ASSIGNMENT OF ASSIGNORS INTEREST;ASSIGNOR:ALKAYALI, AHMED;REEL/FRAME:029219/0587 Effective date: 19971202 |
|
FPAY | Fee payment |
Year of fee payment: 12 |